Investigation of the Thermostable Branched‐Chain Transaminase From <i>Aeribacillus pallidus</i> : Identification, Characterization, and Application
A yet unidentified branched-chain transaminase (BCAT), ApBCAT, was identified in the thermostable Aeribacillus pallidus. Notably, ApBCAT exhibits exceptional thermal stability and demonstrates the ability to catalyze a wide range of natural and unnatural amino acids. This combination of broad substrate spectrum and thermal resistance is unusual in the BCAT family, indicating the promising industrial potential of ApBCAT.
Authors
- Chuanzhi Zhang
- Shaojie Ma (ORCID: https://orcid.org/0000-0002-8782-3047)
- Chaoyong James Yang (ORCID: https://orcid.org/0000-0002-2374-5342)
- Da‐Hua Shi (ORCID: https://orcid.org/0000-0002-3101-0418)
- Min Zheng (ORCID: https://orcid.org/0000-0001-9148-7544)
- Jiahuan Li (ORCID: https://orcid.org/0000-0002-0743-4958)
- Tingting Li (ORCID: https://orcid.org/0000-0003-4266-0317)
- Xiaole Yang
Institutions
- Kanion Pharmaceutical (China) (CN)
- Lianyungang Runzhong Pharmaceutical (China) (CN)
Publication Details
- Journal
- Chemistry & Biodiversity
- Published
- 2025-04-15
- DOI
- https://doi.org/10.1002/cbdv.202500678
- Primary Topic
- Chemical Synthesis and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- China Postdoctoral Science Foundation
- Jiangsu Ocean University